VprBP

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(New page: <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> == Function == '''VPRBP''' (VPR-binding protein) is a HIV-1 WD40 protein is essentia...)
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<StructureSection load='5jk7' size='350' side='right' caption='Human VprBP residues 1045-1396 (pink) complex with Vpr (cyan), DNA damage-binding protein (green) and uracil-DNA glycosylase (yellow) (PDB code [[5jk7]])' scene='77/776391/Cv/2'>
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''>
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== Function ==
== Function ==
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'''VPRBP''' (VPR-binding protein) is a HIV-1 WD40 protein is essential for DNA replication and embryonic development<ref>PMID:18606781</ref>. VPRBP has intrinsic kinase activity and is capable of phosphorylating histone H2A. Recruitment of VPRBP by VPR is essential for HIV-1 VPR activity of initiating the host cell response cycle arresting its G(2) phase following mitosis<ref>PMID:17314515</ref>.
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'''VprBP''' ('''VPR-binding protein''') or '''DDB1- and CUL4-associated factor 1''' or '''DCAF1''' is a HIV-1 WD40 protein is essential for DNA replication and embryonic development<ref>PMID:18606781</ref>. VprBP has intrinsic kinase activity and is capable of phosphorylating histone H2A. Recruitment of VprBP by Vpr is essential for HIV-1 VPR activity of initiating the host cell response cycle arresting its G(2) phase following mitosis<ref>PMID:17314515</ref>. VprBP interacts with merlin which is then recruited to the E3 ligase complex resulting in its polyubiquitination and consequently its proteasome-mediated degradation<ref>PMID:18332868</ref>.
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== Disease ==
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== Relevance ==
== Relevance ==
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VPRBP inhibition could be a strategy for the development of anticancer therapeutics<ref>PMID:24140421</ref>.
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VprBP inhibition could be a strategy for the development of anticancer therapeutics<ref>PMID:24140421</ref>.
== Structural highlights ==
== Structural highlights ==
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The interactions between VprBP and Vpr are located in a cleft formed by <scene name='77/776391/Cv/10'>VprBD canonical WD40 seven-blade β-propeller</scene> ({{Template:ColorKey_Helix}}, {{Template:ColorKey_Strand}}, {{Template:ColorKey_Loop}}, {{Template:ColorKey_Turn}}) which is <scene name='77/776391/Cv/11'>lined by acidic residues on one end and hydrophobic residues at the center</scene> ({{Template:ColorKey_Charge_Anionic}} / {{Template:ColorKey_Charge_Cationic}}; {{Template:ColorKey_Hydrophobic}}, {{Template:ColorKey_Polar}}). The interactions are formed by <scene name='77/776391/Cv/12'>hydrogen bonds</scene>, <scene name='77/776391/Cv/13'>Vpr Phe residue buried in VprBP hydrophobic pocket</scene> and <scene name='77/776391/Cv/14'>VprBP Trp binding to residues in Vpr pocket</scene><ref>PMID:27571178</ref>.
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</StructureSection>
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== 3D Structures of VprBP ==
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== 3D Structures of VPRBP ==
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[[VprBP 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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[[4pxw]] – hVPRBP residues 1039-1401 (mutant) - human <br />
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[[3wa0]] – hVPRBP residues 1417-1506 + merlin <br />
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[[4p7i]] – hVPRBP residues 998-1058 + merlin <br />
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[[4z8l]], [[5aja]], [[4cc9]] – hVPRBP residues 1057-1396 + VPX + SAMHD1 <br />
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[[5jk7]] – hVPRBP residues 1045-1396 + VPR + DNA damage-binding protein + uracil-DNA glycosylase <br />
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Human VprBP residues 1045-1396 (pink) complex with Vpr (cyan), DNA damage-binding protein (green) and uracil-DNA glycosylase (yellow) (PDB code 5jk7)

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Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel, Jaime Prilusky

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